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Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
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Rationally designed stapled peptides allosterically inhibit PTBP1-RNA-binding.

Stefan Schmeing1, Gulshan Amrahova1, Katrin Bigler1

  • 1Chemical Genomics Centre of the Max Planck Society, Max Planck Institute of Molecular Physiology Otto-Hahn-Strasse 11 44227 Dortmund Germany peter.t-hart@mpi-dortmund.mpg.de.

Chemical Science
|August 11, 2023
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Summary
This summary is machine-generated.

Scientists developed novel stapled peptide inhibitors targeting the splicing factor PTBP1. These cell-permeable inhibitors block RNA binding by mimicking a transient helix, offering a new therapeutic strategy for PTBP1-driven diseases.

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Area of Science:

  • Molecular Biology
  • Drug Discovery
  • Structural Biology

Background:

  • The splicing factor PTBP1 plays a critical role in human cellular processes and disease development.
  • PTBP1's RNA-binding mechanism, mediated by RNA-recognition motifs, lacks conventional inhibitory pockets.
  • A transient helix within PTBP1's first RNA-recognition motif is crucial for RNA binding.

Purpose of the Study:

  • To investigate the dynamic nature of the PTBP1 transient helix for therapeutic targeting.
  • To develop and validate stapled peptide inhibitors against PTBP1.
  • To demonstrate the potential of mimicking transient protein structures for drug development.

Main Methods:

  • Protein crystallography to visualize inhibitor binding.
  • Fluorescence polarization assays to measure RNA binding inhibition.
  • Cell-based assays (in cellulo) to assess splicing regulation changes.

Main Results:

  • Stapled peptides were designed to inhibit PTBP1's RNA binding.
  • Inhibitors were confirmed to bind to the transient helix site.
  • Validated cell-permeable inhibitors altered PTBP1-regulated alternative splicing.

Conclusions:

  • Transient protein secondary structures can be mimicked by stapled peptides for inhibition.
  • This approach offers a novel strategy for targeting allosteric mechanisms.
  • Stapled peptides represent a promising class of inhibitors for diseases driven by PTBP1.